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Information on EC 2.1.1.276 - gibberellin A4 carboxyl methyltransferase
for references in articles please use BRENDA:EC2.1.1.276
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.276 gibberellin A4 carboxyl methyltransferase
IUBMB Comments
The enzyme also methylates gibberellins A34 (80%), A9 (60%), and A3 (45%) with significant activity.
The expected taxonomic range for this enzyme is: Arabidopsis thaliana
Reaction Schemes
showSynonyms
gamt2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GAMT2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + gibberellin A4 = S-adenosyl-L-homocysteine + methyl gibberellin A4
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
gibberellin inactivation II (methylation)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:gibberellin A4 O-methyltransferase
The enzyme also methylates gibberellins A34 (80%), A9 (60%), and A3 (45%) with significant activity.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + gibberellin A1
S-adenosyl-L-homocysteine + methyl gibberellin A1
Substrates: 30% of the activity compared to methylation of gibberellin A4
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A20
S-adenosyl-L-homocysteine + methyl gibberellin A20
Substrates: 15% of the activity compared to methylation of gibberellin A4
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A3
O-methyl gibberellin A3 + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + gibberellin A3
S-adenosyl-L-homocysteine + methyl gibberellin A3
Substrates: 45% of the activity compared to methylation of gibberellin A4
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A34
S-adenosyl-L-homocysteine + methyl gibberellin A34
Substrates: 80% of the activity compared to methylation of gibberellin A4
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A4
S-adenosyl-L-homocysteine + methyl gibberellin A4
S-adenosyl-L-methionine + gibberellin A51
S-adenosyl-L-homocysteine + methyl gibberellin A51
Substrates: 16% of the activity compared to methylation of gibberellin A4
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A9
S-adenosyl-L-homocysteine + methyl gibberellin A9
Substrates: 60% of the activity compared to methylation of gibberellin A4
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A3
O-methyl gibberellin A3 + S-adenosyl-L-homocysteine
-
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A3
O-methyl gibberellin A3 + S-adenosyl-L-homocysteine
-
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A4
S-adenosyl-L-homocysteine + methyl gibberellin A4
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + gibberellin A4
S-adenosyl-L-homocysteine + methyl gibberellin A4
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Substrates: -
Products: -
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additional information
?
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Substrates: no activity with gibberelin A12 and gibberelin A19
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additional information
?
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Substrates: no activity with gibberelin A12 and gibberelin A19
Products: -
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?
additional information
?
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Substrates: the enzyme does not methylate abscisic acid
Products: -
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additional information
?
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Substrates: the enzyme does not methylate abscisic acid
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + gibberellin A3
O-methyl gibberellin A3 + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + gibberellin A4
S-adenosyl-L-homocysteine + methyl gibberellin A4
S-adenosyl-L-methionine + gibberellin A3
O-methyl gibberellin A3 + S-adenosyl-L-homocysteine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + gibberellin A3
O-methyl gibberellin A3 + S-adenosyl-L-homocysteine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + gibberellin A4
S-adenosyl-L-homocysteine + methyl gibberellin A4
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + gibberellin A4
S-adenosyl-L-homocysteine + methyl gibberellin A4
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not methylate abscisic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not methylate abscisic acid
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
not enhanced nor inhibited by K+, NH4+, Na+, Ca2+, Fe2þ, Mg2+, and Mn2+
additional information
-
not enhanced nor inhibited by K+, NH4+, Na+, Ca2+, Fe2þ, Mg2+, and Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
GAMT2 null mutant shows reduced inhibition of germination, compared with the wild type, when placed on plates containing the gibberellin biosynthesis inhibitor ancymidol
malfunction
-
a GAMT2null mutant displays ancymidol- and abscisic acid-resistant phenotype in seed germination assay
malfunction
-
loss of enzyme function leads to early flowering, whereas transgenic misexpression of the enzyme in specific regions around the shoot apical meristem delays flowering
malfunction
-
a GAMT2null mutant displays ancymidol- and abscisic acid-resistant phenotype in seed germination assay
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physiological function
methylation of gibberellins by the enzyme serves to deactivate gibberellins and initiate their degradation as the seeds mature
physiological function
-
the enzyme is involved in seed maturation, germination and silique development by modulating gibberellic acid activity. Enzyme overexpression in Arabidopsis results in multiple phenotypes, including dwarfism, retarded growth, late flowering, and reduced fertility
physiological function
-
the enzyme is a repressor of flowering that may act as a buffer of gibberellic acid levels at the shoot apical meristem to help prevent premature flowering
physiological function
-
the enzyme is involved in seed maturation, germination and silique development by modulating gibberellic acid activity. Enzyme overexpression in Arabidopsis results in multiple phenotypes, including dwarfism, retarded growth, late flowering, and reduced fertility
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, expression in Arabidopsis thaliana under the control of the 35S cauliflower mosaic virus promoter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during seed germination, the expression of the enzyme decreases until the cotyledons expand out of the seed coat
expressed mainly in whole siliques, peak transcript levels from the middle until the end of silique development
the enzyme expression is strongly increased by the application of exogenous gibberellic acid
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the enzyme is significantly upregulated at the SAM during floral transition
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during seed germination, the expression of the enzyme decreases until the cotyledons expand out of the seed coat
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during seed germination, the expression of the enzyme decreases until the cotyledons expand out of the seed coat
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-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Varbanova, M.; Yamaguchi, S.; Yang, Y.; McKelvey, K.; Hanada, A.; Borochov, R.; Yu, F.; Jikumaru, Y.; Ross, J.; Cortes, D.; Ma, C.J.; Noel, J.P.; Mander, L.; Shulaev, V.; Kamiya, Y.; Rodermel, S.; Weiss, D.; Pichersky, E.
Methylation of gibberellins by Arabidopsis GAMT1 and GAMT2
Plant Cell
19
32-45
2007
Arabidopsis thaliana (Q5XF78), Arabidopsis thaliana
brenda
Xing, S.; Qin, G.; Shi, Y.; Ma, Z.; Chen, Z.; Gu, H.; Qu, L.
GAMT2 encodes a methyltransferase of gibberellic acid that is involved in seed maturation and germination in Arabidopsis
J. Integr. Plant Biol.
49
368-381
2007
Arabidopsis thaliana, Arabidopsis thaliana ecotype Columbia-0
-
brenda
Lee, J.E.; Goretti, D.; Neumann, M.; Schmid, M.; You, Y.
A gibberellin methyltransferase modulates the timing of floral transition at the Arabidopsis shoot meristem
Physiol. Plant.
170
474-487
2020
Arabidopsis thaliana
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.276)
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Release 2026.1 (March 2026)
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